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  Protein Correlation Profiles Identify Lipid Droplet Proteins with High Confidence

Krahmer, N., Hilger, M., Kory, N., Wilfling, F., Stoehr, G., Mann, M., et al. (2013). Protein Correlation Profiles Identify Lipid Droplet Proteins with High Confidence. MOLECULAR & CELLULAR PROTEOMICS, 12(5), 1115-1126. doi:10.1074/mcp.M112.020230.

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Krahmer, Natalie1, Autor           
Hilger, Maximiliane2, Autor           
Kory, Nora1, Autor
Wilfling, Florian1, Autor
Stoehr, Gabriele2, Autor           
Mann, Matthias2, Autor           
Farese Jr., Robert V.1, Autor
Walther, Tobias C.1, Autor           
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Schlagwörter: SPECTROMETRY-BASED PROTEOMICS; QUANTITATIVE PROTEOMICS; ENDOPLASMIC-RETICULUM; DROSOPHILA; SILAC; MITOCHONDRIA; MEMBRANE; REVEALS; QUANTIFICATION; TRANSLOCATION
 Zusammenfassung: Lipid droplets (LDs) are important organelles in energy metabolism and lipid storage. Their cores are composed of neutral lipids that form a hydrophobic phase and are surrounded by a phospholipid monolayer that harbors specific proteins. Most well-established LD proteins perform important functions, particularly in cellular lipid metabolism. Morphological studies show LDs in close proximity to and interacting with membrane-bound cellular organelles, including the endoplasmic reticulum, mitochondria, peroxisomes, and endosomes. Because of these close associations, it is difficult to purify LDs to homogeneity. Consequently, the confident identification of bona fide LD proteins via proteomics has been challenging. Here, we report a methodology for LD protein identification based on mass spectrometry and protein correlation profiles. Using LD purification and quantitative, high-resolution mass spectrometry, we identified LD proteins by correlating their purification profiles to those of known LD proteins. Application of the protein correlation profile strategy to LDs isolated from Drosophila S2 cells led to the identification of 111 LD proteins in a cellular LD fraction in which 1481 proteins were detected. LD localization was confirmed in a subset of identified proteins via microscopy of the expressed proteins, thereby validating the approach. Among the identified LD proteins were both well-characterized LD proteins and proteins not previously known to be localized to LDs. Our method provides a high-confidence LD proteome of Drosophila cells and a novel approach that can be applied to identify LD proteins of other cell types and tissues.

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Sprache(n): eng - English
 Datum: 2013-05
 Publikationsstatus: Erschienen
 Seiten: 12
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000319705100006
DOI: 10.1074/mcp.M112.020230
 Art des Abschluß: -

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Titel: MOLECULAR & CELLULAR PROTEOMICS
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Seiten: - Band / Heft: 12 (5) Artikelnummer: - Start- / Endseite: 1115 - 1126 Identifikator: ISSN: 1535-9476